Reorientational Dynamics of Amyloid-β from NMR Spin Relaxation and Molecular Simulation.

ABSTRACT: Amyloid-β (Aβ) aggregation is a hallmark of Alzheimer's disease. As an intrinsically disordered protein, Aβ undergoes extensive dynamics on multiple length and time scales. Access to a comprehensive picture of the reorientational dynamics in Aβ requires therefore the combination of complementary techniques. Here, we integrate ¹⁵N spin relaxation rates at three magnetic fields with microseconds-long molecular dynamics simulation, ensemble-based hydrodynamic calculations, and previously published nanosecond fluorescence correlation spectroscopy to investigate the reorientational dynamics of Aβ1-40 (Aβ40) at single-residue resolution. The integrative analysis shows that librational and dihedral angle fluctuations occurring at fast and intermediate time scales are not sufficient to

SUBMITTER: Rezaei-Ghaleh N 

PROVIDER: S-EPMC6598774 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature